[HTML][HTML] The peptides acetyl-(Gly-3 (S) Hyp-4 (R) Hyp) 10-NH2 and acetyl-(Gly-Pro-3 (S) Hyp) 10-NH2 do not form a collagen triple helix
Hydroxylation of proline residues in the Yaa position of the Gly-Xaa-Yaa repeated sequence
to 4 (R)-hydroxyproline is essential for the formation of the collagen triple helix. A small
number of 3 (S)-hydroyxyproline residues are present in most collagens in the Xaa position.
Neither the structural nor a biological role is known for 3 (S)-hydroxyproline. To characterize
the structural role of 3 (S)-hydroxyproline, the peptide Ac-(Gly-3 (S) Hyp-4 (R) Hyp) 10-NH 2
was synthesized and analyzed by circular dichroism spectroscopy, analytical …
to 4 (R)-hydroxyproline is essential for the formation of the collagen triple helix. A small
number of 3 (S)-hydroyxyproline residues are present in most collagens in the Xaa position.
Neither the structural nor a biological role is known for 3 (S)-hydroxyproline. To characterize
the structural role of 3 (S)-hydroxyproline, the peptide Ac-(Gly-3 (S) Hyp-4 (R) Hyp) 10-NH 2
was synthesized and analyzed by circular dichroism spectroscopy, analytical …